Literature summary extracted from
Yu, H.; Zhao, S.; Guo, L.
Novel Gene encoding 5-aminosalicylate 1,2-dioxygenase from Comamonas sp. strain QT12 and catalytic properties of the purified enzyme (2018), J. Bacteriol., 200, e00395-17 .
Cloned(Commentary)
EC Number |
Cloned (Comment) |
Organism |
---|
1.13.11.86 |
heterologously expressed in Escherichia coli as a His-tagged enzyme |
Comamonas thiooxydans |
Protein Variants
EC Number |
Protein Variants |
Comment |
Organism |
---|
1.13.11.86 |
G93A |
the mutant enzyme shows the ability to oxidize salicylate, the wild-type enzyme shows no activity with salicylate |
Comamonas thiooxydans |
1.13.11.86 |
H107A |
mutant enzyme shows no enzymatic activity |
Comamonas thiooxydans |
1.13.11.86 |
H109A |
mutant enzyme shows no enzymatic activity |
Comamonas thiooxydans |
1.13.11.86 |
H150A |
mutant enzyme shows no enzymatic activity |
Comamonas thiooxydans |
Inhibitors
EC Number |
Inhibitors |
Comment |
Organism |
Structure |
---|
1.13.11.86 |
1,10-phenanthroline |
0.01 mM, 89% inhibition |
Comamonas thiooxydans |
|
1.13.11.86 |
EDTA |
1 mM, 31% inhibition |
Comamonas thiooxydans |
|
1.13.11.86 |
SDS |
1 mM, complete inhibition |
Comamonas thiooxydans |
|
KM Value [mM]
EC Number |
KM Value [mM] |
KM Value Maximum [mM] |
Substrate |
Comment |
Organism |
Structure |
---|
1.13.11.86 |
0.052 |
- |
5-Aminosalicylate |
pH 8.0, 25°C, wild-type enzyme |
Comamonas thiooxydans |
|
1.13.11.86 |
0.823 |
- |
gentisate |
pH 8.0, 25°C, wild-type enzyme |
Comamonas thiooxydans |
|
Metals/Ions
EC Number |
Metals/Ions |
Comment |
Organism |
Structure |
---|
1.13.11.86 |
Fe2+ |
required for the catalytic activity of the purified enzyme, nonheme iron dioxygenase. The enzyme activity of MabB increases about 2.3fold with the addition of 0.25 mM Fe2+, and 74% enzyme activity is observed when 0.25 mM Fe3+ is added |
Comamonas thiooxydans |
|
Molecular Weight [Da]
EC Number |
Molecular Weight [Da] |
Molecular Weight Maximum [Da] |
Comment |
Organism |
---|
1.13.11.86 |
45000 |
- |
SDS-PAGE |
Comamonas thiooxydans |
Natural Substrates/ Products (Substrates)
EC Number |
Natural Substrates |
Organism |
Comment (Nat. Sub.) |
Natural Products |
Comment (Nat. Pro.) |
Rev. |
Reac. |
---|
1.13.11.86 |
5-aminosalicylate + O2 |
Comamonas thiooxydans |
the enzyme plays an important physiological role in 3-aminobenzoate degradation in Comamonas sp. strain QT12 |
(2Z,4E)-4-amino-6-oxohepta-2,4-dienedioate |
- |
? |
|
Organism
EC Number |
Organism |
UniProt |
Comment |
Textmining |
---|
1.13.11.86 |
Comamonas thiooxydans |
A0A1V0ELS9 |
- |
- |
Purification (Commentary)
EC Number |
Purification (Comment) |
Organism |
---|
1.13.11.86 |
- |
Comamonas thiooxydans |
Substrates and Products (Substrate)
EC Number |
Substrates |
Comment Substrates |
Organism |
Products |
Comment (Products) |
Rev. |
Reac. |
---|
1.13.11.86 |
1-hydroxy-2-naphthoate + O2 |
oxidized by MabB at a rate less than 1% of that observed for 5-aminosalicylate |
Comamonas thiooxydans |
(3Z)-4-(2-carboxyphenyl)-2-oxobut-3-enoate |
- |
? |
|
1.13.11.86 |
5-aminosalicylate + O2 |
the enzyme plays an important physiological role in 3-aminobenzoate degradation in Comamonas sp. strain QT12 |
Comamonas thiooxydans |
(2Z,4E)-4-amino-6-oxohepta-2,4-dienedioate |
- |
? |
|
1.13.11.86 |
5-aminosalicylate + O2 |
the two oxygen atoms incorporated into the product are both from the dioxygen molecule. Both 5-aminosalicylate and gentisate can be converted by MabB. The catalytic efficiency of MabB for 5-aminosalicylate is much higher (about 70fold) than that for gentisate |
Comamonas thiooxydans |
(2Z,4E)-4-amino-6-oxohepta-2,4-dienedioate |
- |
? |
|
1.13.11.86 |
gentisate + O2 |
the two oxygen atoms incorporated into the product are both from the dioxygen molecule. Both 5-aminosalicylate and gentisate can be converted by MabB. The catalytic efficiency of MabB for 5-aminosalicylate is much higher (about 70fold) than that for gentisate |
Comamonas thiooxydans |
maleylpyruvate |
- |
? |
|
1.13.11.86 |
additional information |
no activity is detected in reaction with salicylate |
Comamonas thiooxydans |
? |
- |
? |
|
Subunits
EC Number |
Subunits |
Comment |
Organism |
---|
1.13.11.86 |
? |
x * 45000, SDS-PAGE |
Comamonas thiooxydans |
Synonyms
EC Number |
Synonyms |
Comment |
Organism |
---|
1.13.11.86 |
mabB |
- |
Comamonas thiooxydans |
Temperature Optimum [°C]
EC Number |
Temperature Optimum [°C] |
Temperature Optimum Maximum [°C] |
Comment |
Organism |
---|
1.13.11.86 |
10 |
- |
- |
Comamonas thiooxydans |
Temperature Range [°C]
EC Number |
Temperature Minimum [°C] |
Temperature Maximum [°C] |
Comment |
Organism |
---|
1.13.11.86 |
10 |
45 |
10°C: maximal activity, 45°C: about 60% of maximal activity |
Comamonas thiooxydans |
pH Optimum
EC Number |
pH Optimum Minimum |
pH Optimum Maximum |
Comment |
Organism |
---|
1.13.11.86 |
7.5 |
8 |
- |
Comamonas thiooxydans |
pH Range
EC Number |
pH Minimum |
pH Maximum |
Comment |
Organism |
---|
1.13.11.86 |
6.5 |
9 |
pH 6.5: about 50% of maximal activity, pH 9.0: about 40% of maximal activity |
Comamonas thiooxydans |
Expression
EC Number |
Organism |
Comment |
Expression |
---|
1.13.11.86 |
Comamonas thiooxydans |
the enzyme is induced by 3-aminobenzoate or its degradation intermediates |
up |
General Information
EC Number |
General Information |
Comment |
Organism |
---|
1.13.11.86 |
malfunction |
the mabB-disrupted mutant loses the ability to grow on 3-aminobenzoate |
Comamonas thiooxydans |
1.13.11.86 |
metabolism |
the enzyme plays an important physiological role in 3-aminobenzoate degradation in Comamonas sp. strain QT12 |
Comamonas thiooxydans |